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2YXT

Human Pyridoxal Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008478molecular_functionpyridoxal kinase activity
A0009443biological_processpyridoxal 5'-phosphate salvage
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0030170molecular_functionpyridoxal phosphate binding
A0030955molecular_functionpotassium ion binding
A0031402molecular_functionsodium ion binding
A0031403molecular_functionlithium ion binding
A0034774cellular_componentsecretory granule lumen
A0035580cellular_componentspecific granule lumen
A0042803molecular_functionprotein homodimerization activity
A0042817biological_processpyridoxal metabolic process
A0042818biological_processpyridoxamine metabolic process
A0042822biological_processpyridoxal phosphate metabolic process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0008478molecular_functionpyridoxal kinase activity
B0009443biological_processpyridoxal 5'-phosphate salvage
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0030170molecular_functionpyridoxal phosphate binding
B0030955molecular_functionpotassium ion binding
B0031402molecular_functionsodium ion binding
B0031403molecular_functionlithium ion binding
B0034774cellular_componentsecretory granule lumen
B0035580cellular_componentspecific granule lumen
B0042803molecular_functionprotein homodimerization activity
B0042817biological_processpyridoxal metabolic process
B0042818biological_processpyridoxamine metabolic process
B0042822biological_processpyridoxal phosphate metabolic process
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1314
ChainResidue
AASP113
AHOH1320
AHOH1321
AHOH1322
AHOH1323
AHOH1324

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 1316
ChainResidue
BHOH1352
BHOH1353
BTHR186
BHOH1350
BHOH1351

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 1319
ChainResidue
AGLN63
AARG70
AMET93
AGLU100
AHOH1451

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1329
ChainResidue
BGLY32
BHIS246
BLYS247
BHOH1582

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 1335
ChainResidue
BILE223
BARG224

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1337
ChainResidue
BGLY179
BASP181
BHOH1384
BHOH1385

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 1347
ChainResidue
BGLU155
BLYS161

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 1349
ChainResidue
BGLN63
BTYR66
BARG70
BASP96
BGLU100

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 1001
ChainResidue
ASER12
ATHR47
AHOH1365
AHOH1441
AHOH1478

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 1003
ChainResidue
ATHR186
AGLY234
ALEU263

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 1005
ChainResidue
AARG224
AHIS264
AGLN268

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 1009
ChainResidue
AGLY32
AHIS246
ALYS247
AHOH1536

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 1013
ChainResidue
AILE223
AARG224

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD B 1023
ChainResidue
BTHR186
BHOH1497

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 1025
ChainResidue
BILE223
BARG224
BHIS264
BGLN268

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD B 1027
ChainResidue
BASP181

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 1031
ChainResidue
BSER12
BHIS46
BTHR47
BHOH1455

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 1033
ChainResidue
BPHE43
BTYR84
BARG86

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 1039
ChainResidue
BGLU130
BLEU156
BHOH1496
BHOH1502

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 1041
ChainResidue
BSER177
BARG206
BLEU312

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 1045
ChainResidue
BTHR47
BTYR84
BTYR127

site_idCC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD B 1053
ChainResidue
BGLN205
BTHR245
BPRO249
BHOH1392
BHOH1428
BHOH1437
BHOH1574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:19351586
ChainResidueDetails
AASP235
BASP235

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0007744|PDB:3FHX
ChainResidueDetails
ASER12
BSER12

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.16, ECO:0007744|PDB:3KEU
ChainResidueDetails
ATHR47
BTHR47

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:4EN4
ChainResidueDetails
AASP113
BASP113

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
AASP118
BASP118

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:2YXT, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
ATHR148
ATHR186
BTHR148
BTHR186

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHY, ECO:0007744|PDB:3KEU
ChainResidueDetails
AASN150
BASN150

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
AVAL226
BVAL226

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:2YXU, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3FHY, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
ATHR233
BTHR233

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU
ChainResidueDetails
AGLY234
BGLY234

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P82197
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER59
ASER164
BSER59
BSER164

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER213
BSER213

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER285
BSER285

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
AGLY234
ATHR233
AGLY232
AASP235

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
BGLY234
BTHR233
BGLY232
BASP235

237992

PDB entries from 2025-06-25

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